Activin AB ELISA

Activins, like all members of the transforming growth factor-beta superfamily, are synthesized as large pro-hormones with N-terminal pro- and C-terminal mature domains. Studies have shown that the prodomains template the dimerization of pro-activin forms, that are subsequently processed to yield pro/mature fragments. The prodomains, although important for folding and extracellular localization, must be removed prior to activity. Activin forms retaining the prodomain are biologically inactive. Recombinant Human Activin AB is produced from a DNA sequence encoding human Activin βA chain and human βB chain. Activin AB is expressed in CHO (Chinese Hamster Ovary) cells. Recombinant human mature Activin AB, generated by the proteolytic removal of the propeptides, is a disulfide-linked heterodimer of the mature human Activin βA chain and mature human Activin βB chain. Based on N-terminal sequencing, the βA chain starts at Gly 311 and the βB chain starts at Gly 293. The A and B monomers of recombinant human Activin AB have the same apparent molecular mass of approximately 14 kDa in SDS-PAGE under reducing conditions.